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001-es BibID:	BIBFORM003891
Első szerző:	Gyémánt Gyöngyi (vegyész)
Cím:	Evidence for pentagalloyl glucose binding to human salivary α-amylase through aromatic amino acid residues / Gyöngyi Gyémánt, Ágnes Zajácz, Bálint Bécsi, Chandran Ragunath, Narayanan Ramasubbu, Ferenc Erdődi, Gyula Batta, Lili Kandra
Dátum:	2009
ISSN:	1570-9639
Megjegyzések:	We demonstrate here that pentagalloyl glucose (PGG), a main component of gallotannins, was an effective inhibitor of HSA and it exerted similar inhibitory potency to Aleppo tannin used in this study. The inhibition of HSA by PGG was found to be non-competitive and inhibitory constants of KEI = 2.6 ?M and KESI = 3.9 ?M were determined from Lineweaver-Burk secondary plots. PGG as a model compound for gallotannins was selected to study the inhibitory mechanism and to characterize the interaction of HSA with this type of molecules. Surface plasmon resonance (SPR) binding experiments confirmed the direct interaction of HSA and PGG, and it also established similar binding of Aleppo tannin to HSA. Saturation transfer difference (STD) experiment by NMR clearly demonstrated the aromatic rings of PGG may be involved in the interaction suggesting a possible stacking with the aromatic side chains of HSA. The role of aromatic amino acids of HSA in PGG binding was reinforced by kinetic studies with the W58L and Y151M mutants of HSA: the replacement of the active site aromatic amino acids with aliphatic ones decreased the PGG inhibition dramatically, which justified the importance of these residues in the interaction.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Molekulatudomány pentagalloyl glucose human salivary alpha-amylase inhibition surface plasmon resonance saturation transfer difference NMR
Megjelenés:	Biochimica et Biophysica Acta (BBA). Proteins and Proteomics. - 1794 : 2 (2009), p. 291-296. -
További szerzők:	Zajácz Ágnes Bécsi Bálint (1981-) (vegyészmérnök) Ragunath, Chandran Ramasubbu, Narayanan Erdődi Ferenc (1953-) (biokémikus) Batta Gyula (1953-) (molekula-szerkezet kutató) Kandra Lili (1943-) (biokémikus)
Pályázati támogatás:	TÁMOP-4.2.2-08/1-2008-0019 TÁMOP
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI Szerző által megadott URL
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001-es BibID:	BIBFORM003913
Első szerző:	Mádi András (biológus)
Cím:	Mass spectrometric proteome analysis suggests anaerobic shift in metabolism of Dauer larvae of Caenorhabditis elegans / András Mádi, Stefan Mikkat, Cornelia Koy, Bruno Ringel, Hans-Jürgen Thiesen, Michael O. Glocker
Dátum:	2008
ISSN:	1570-9639
Megjegyzések:	The Dauer larva is a non-feeding alternative larval stage of some nematodes specialized for long-term survival and dispersal. In this study we compared proteome maps obtained from Dauer larvae with those from the corresponding third larval stage (L3) of the feeding life cycle of C. elegans wild-type strain N2. We demonstrate at the protein level that altered metabolism may participate in longevity determination of Dauers. We detected huge amounts of alcohol dehydrogenase (CE12212) and aldehyde dehydrogenase (CE29809) in Dauer animals, indicating highly active fermentative pathways. Inorganic pyrophosphatase (CE05448) that enables to metabolize pyrophosphate as a high-energy source was over-expressed in Dauers. An interesting differentially expressed protein was phosphatidylethanolamine-binding protein (CE38516) that was found in high abundance in samples from Dauer larvae. Protein synthesis may be lowered in Dauer animals by the reduced expression of splicing factor rsp-3 (CE31089) and methionyl-tRNA synthase (CE34219). We observed significantly lower amounts of the pepsin-like aspartyl protease 1 (CE21681) in non-feeding Dauers, which is in agreement with reduced nutrient digestion. Finally, the hypothetical protein R08E5.2 (CE33294) was present in high abundance in L3 animals.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Metabolism Fractionated protein extraction Proteomics MALDI ToF MS C. elegans
Megjelenés:	Biochimica et Biophysica Acta (BBA). Proteins and Proteomics. - 1784 : 11 (2008), p. 1763-1770. -
További szerzők:	Mikkat, Stefan Koy, Cornelia Ringel, Bruno Thiesen, Hans-Jürgen Glocker, Michael O.
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI Szerző által megadott URL
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